Interaction between heterologous receptor tyrosine kinases

FEBS Letters

Tartare, Sophie¹  Ballotti, Robert¹  Van Obberghen, Emmanuel¹ 

[1] Institut National de la Santé et de la Recherche Médicale, INSERM U145, Faculté de Médecine, 06107 Nice, Cédex 2, France

关键词: Insulin receptor;    IGF-I receptor;    Phosphorylation;    Tyrosine kinase;    IGF-I;    insulin-like Growth Factor-I;    CSF-I;    colony-stimulating growth factor-I;    PDGF;    platelet derived growth factor;    EGF;    epidermal growth factor;    EDTA;    ethylenediaminetetraacetic acid;    HEPES;    N-2-hydroxyethylpiperazine-N′-2-ethane sulfonic acid;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(91)81422-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To determine whether heterologous receptor tyrosine kinases interact with each other we have investigated the ability of insulin receptors to transphosphorylate and transactivate IGF-I receptors. Using partially purified receptors we show that hormone-stimulated insulin receptors induced a 40% increase in IGF-I receptor phosphorylation. Remarkably, this transphosphorylation of IGF-I receptors by insulin receptors resulted in a 2.5-fold augmentation of the IGF-I receptor tyrosine kinase activity for substrates. Our findings demonstrate that transphosphorylation with transactivation can occur between insulin and IGF-I receptors. We would like to propose that such a phenomenon participates in the insulin-induced pleiotropic program by mediating the growth promoting effects of the hormone.

【 授权许可】

Unknown